Hemeproteins and model hemes will be examined by magnetic circular dichroism spectroscopy and resonant-Raman spectroscopy. The former technique yields information on the oxidation states of hydroperoxidase compounds I and II. The latter technique will be examined for influence of axial ligands on positions and degree of polarization of the scattered light. X-ray studies of CO and NO heme complexes are being performed. Epr results of the cobalt (II) horseradish peroxidase will be used to determine the local symmetry in this species. The SCF-X alpha technique is being adapted to study transition metal complexes. Model tetraanthracenyl-porphyrins are being synthesized and studied for their oxygen carrying ability. Polarographic studies on water-soluble porphyrins will be employed to ascertain the influence of solvation on redox potentials.